RHG17_HUMAN
ID RHG17_HUMAN Reviewed; 881 AA.
AC Q68EM7; A8K6M6; Q6ZUS4; Q7Z2F2; Q8NDG2; Q96KS2; Q96KS3; Q96SS8; Q9BVF6;
AC Q9H8U5; Q9NW54;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Rho GTPase-activating protein 17;
DE AltName: Full=Rho-type GTPase-activating protein 17;
DE AltName: Full=RhoGAP interacting with CIP4 homologs protein 1;
DE Short=RICH-1;
GN Name=ARHGAP17; Synonyms=RICH1; ORFNames=MSTP066, MSTP110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, AND
RP MUTAGENESIS OF ARG-288.
RX PubMed=11431473; DOI=10.1074/jbc.m103540200;
RA Richnau N., Aspenstroem P.;
RT "Rich, a rho GTPase-activating protein domain-containing protein involved
RT in signaling by Cdc42 and Rac1.";
RL J. Biol. Chem. 276:35060-35070(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5).
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6).
RC TISSUE=Cervix, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881.
RC TISSUE=Aorta;
RA Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y.,
RA Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=11285285; DOI=10.1083/jcb.153.1.191;
RA Reczek D., Bretscher A.;
RT "Identification of EPI64, a TBC/rabGAP domain-containing microvillar
RT protein that binds to the first PDZ domain of EBP50 and E3KARP.";
RL J. Cell Biol. 153:191-206(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, AND INTERACTION WITH AMOT;
RP PALS1; PATJ; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND THR-682, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the maintenance of
CC tight junction by regulating the activity of CDC42, thereby playing a
CC central role in apical polarity of epithelial cells. Specifically acts
CC as a GTPase activator for the CDC42 GTPase by converting it to an
CC inactive GDP-bound state. The complex formed with AMOT acts by
CC regulating the uptake of polarity proteins at tight junctions, possibly
CC by deciding whether tight junction transmembrane proteins are recycled
CC back to the plasma membrane or sent elsewhere. Participates in the
CC Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing
CC GTPase activity of Rho family proteins and by inducing the
CC reorganization of the cortical actin filaments. Acts as a GTPase
CC activator in vitro for RAC1. {ECO:0000269|PubMed:11431473,
CC ECO:0000269|PubMed:16678097}.
CC -!- SUBUNIT: Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1,
CC TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and
CC SH3KBP1/CIN85. {ECO:0000269|PubMed:11285285,
CC ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:16678097}.
CC -!- INTERACTION:
CC Q68EM7; Q4VCS5: AMOT; NbExp=2; IntAct=EBI-1642807, EBI-2511319;
CC Q68EM7; Q4VCS5-2: AMOT; NbExp=4; IntAct=EBI-1642807, EBI-3891843;
CC Q68EM7; Q15642: TRIP10; NbExp=3; IntAct=EBI-1642807, EBI-739936;
CC Q68EM7; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-1642807, EBI-6550597;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm.
CC Cell junction, tight junction. Note=Associates with membranes and
CC concentrates at sites of cell-cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q68EM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68EM7-2; Sequence=VSP_023687;
CC Name=3;
CC IsoId=Q68EM7-3; Sequence=VSP_023683;
CC Name=4; Synonyms=RICH1B;
CC IsoId=Q68EM7-4; Sequence=VSP_023684, VSP_023685;
CC Name=5;
CC IsoId=Q68EM7-5; Sequence=VSP_023688;
CC Name=6;
CC IsoId=Q68EM7-6; Sequence=VSP_023689;
CC Name=7;
CC IsoId=Q68EM7-7; Sequence=VSP_023682, VSP_023686;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level
CC in heart and placenta. {ECO:0000269|PubMed:11431473}.
CC -!- DOMAIN: The BAR domain mediates the interaction with the coiled coil
CC domain of AMOT, leading to its recruitment to tight junctions.
CC {ECO:0000269|PubMed:16678097}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01241.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAQ13586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAQ13632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ306731; CAC37948.1; -; mRNA.
DR EMBL; AJ306732; CAC37949.1; -; mRNA.
DR EMBL; AK001170; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK023281; BAB14506.1; -; mRNA.
DR EMBL; AK027567; BAB55203.1; -; mRNA.
DR EMBL; AK125358; BAC86144.1; -; mRNA.
DR EMBL; AK291691; BAF84380.1; -; mRNA.
DR EMBL; AL833975; CAD38819.1; -; mRNA.
DR EMBL; BC001241; AAH01241.1; ALT_INIT; mRNA.
DR EMBL; BC080195; AAH80195.1; -; mRNA.
DR EMBL; AF163257; AAQ13586.1; ALT_INIT; mRNA.
DR EMBL; AF173885; AAQ13632.1; ALT_INIT; mRNA.
DR CCDS; CCDS32408.1; -. [Q68EM7-2]
DR CCDS; CCDS32409.1; -. [Q68EM7-1]
DR PIR; F59433; F59433.
DR RefSeq; NP_001006635.1; NM_001006634.2. [Q68EM7-1]
DR RefSeq; NP_060524.4; NM_018054.5. [Q68EM7-2]
DR AlphaFoldDB; Q68EM7; -.
DR SMR; Q68EM7; -.
DR BioGRID; 120424; 72.
DR CORUM; Q68EM7; -.
DR IntAct; Q68EM7; 20.
DR MINT; Q68EM7; -.
DR STRING; 9606.ENSP00000289968; -.
DR GlyGen; Q68EM7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q68EM7; -.
DR MetOSite; Q68EM7; -.
DR PhosphoSitePlus; Q68EM7; -.
DR SwissPalm; Q68EM7; -.
DR BioMuta; ARHGAP17; -.
DR DMDM; 74736331; -.
DR EPD; Q68EM7; -.
DR jPOST; Q68EM7; -.
DR MassIVE; Q68EM7; -.
DR MaxQB; Q68EM7; -.
DR PaxDb; Q68EM7; -.
DR PeptideAtlas; Q68EM7; -.
DR PRIDE; Q68EM7; -.
DR ProteomicsDB; 66129; -. [Q68EM7-1]
DR ProteomicsDB; 66130; -. [Q68EM7-2]
DR ProteomicsDB; 66131; -. [Q68EM7-3]
DR ProteomicsDB; 66132; -. [Q68EM7-4]
DR ProteomicsDB; 66133; -. [Q68EM7-5]
DR ProteomicsDB; 66134; -. [Q68EM7-6]
DR ProteomicsDB; 66135; -. [Q68EM7-7]
DR Antibodypedia; 52174; 182 antibodies from 27 providers.
DR DNASU; 55114; -.
DR Ensembl; ENST00000289968.11; ENSP00000289968.6; ENSG00000140750.17. [Q68EM7-1]
DR Ensembl; ENST00000303665.9; ENSP00000303130.5; ENSG00000140750.17. [Q68EM7-2]
DR Ensembl; ENST00000673196.1; ENSP00000500849.1; ENSG00000288353.1. [Q68EM7-2]
DR Ensembl; ENST00000673560.1; ENSP00000500372.1; ENSG00000288353.1. [Q68EM7-1]
DR GeneID; 55114; -.
DR KEGG; hsa:55114; -.
DR MANE-Select; ENST00000289968.11; ENSP00000289968.6; NM_001006634.3; NP_001006635.1.
DR UCSC; uc002dnb.5; human. [Q68EM7-1]
DR CTD; 55114; -.
DR DisGeNET; 55114; -.
DR GeneCards; ARHGAP17; -.
DR HGNC; HGNC:18239; ARHGAP17.
DR HPA; ENSG00000140750; Low tissue specificity.
DR MIM; 608293; gene.
DR neXtProt; NX_Q68EM7; -.
DR OpenTargets; ENSG00000140750; -.
DR PharmGKB; PA134908575; -.
DR VEuPathDB; HostDB:ENSG00000140750; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000156201; -.
DR HOGENOM; CLU_013806_0_0_1; -.
DR InParanoid; Q68EM7; -.
DR OMA; RLMGCFQ; -.
DR OrthoDB; 821331at2759; -.
DR PhylomeDB; Q68EM7; -.
DR TreeFam; TF350627; -.
DR PathwayCommons; Q68EM7; -.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR SignaLink; Q68EM7; -.
DR BioGRID-ORCS; 55114; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; ARHGAP17; human.
DR GenomeRNAi; 55114; -.
DR Pharos; Q68EM7; Tbio.
DR PRO; PR:Q68EM7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q68EM7; protein.
DR Bgee; ENSG00000140750; Expressed in spleen and 94 other tissues.
DR ExpressionAtlas; Q68EM7; baseline and differential.
DR Genevisible; Q68EM7; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cytoplasm; GTPase activation;
KW Membrane; Phosphoprotein; Reference proteome; SH3-binding; Tight junction.
FT CHAIN 1..881
FT /note="Rho GTPase-activating protein 17"
FT /id="PRO_0000280462"
FT DOMAIN 14..246
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 252..442
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 459..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 753..766
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 522..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..723
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..771
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..818
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 753
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 757
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 759
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 763
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT VAR_SEQ 1..467
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023682"
FT VAR_SEQ 1..273
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023683"
FT VAR_SEQ 215..226
FT /note="LLEAQADYHRKA -> ISGRKNQPLGLP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11431473"
FT /id="VSP_023684"
FT VAR_SEQ 227..881
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11431473"
FT /id="VSP_023685"
FT VAR_SEQ 468..496
FT /note="TGNDSDSGTLERKRPASMAVMEGDLVKKE -> MCGFNTCGPMGFCLSSLLA
FT WCVDCFFSLC (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023686"
FT VAR_SEQ 497..574
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11431473,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_023687"
FT VAR_SEQ 839..881
FT /note="DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL -> GFQNR
FT IAASFLKCTQTQPAKTCLAASCWI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023688"
FT VAR_SEQ 840..881
FT /note="SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL -> V (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023689"
FT MUTAGEN 288
FT /note="R->A: Loss of function; leading to defects in tight
FT junction maintenance."
FT /evidence="ECO:0000269|PubMed:11431473"
FT CONFLICT 139
FT /note="K -> E (in Ref. 2; BAB55203)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Q -> R (in Ref. 1; CAC37948)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="K -> R (in Ref. 1; CAC37948)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="E -> A (in Ref. 2; BAB14506)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="G -> A (in Ref. 2; BAB55203)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="S -> C (in Ref. 2; BAC86144)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="M -> V (in Ref. 2; BAB55203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 881 AA; 95437 MW; 92029DBFFEAD1001 CRC64;
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT
DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV
DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM
DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH
QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL
WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA
AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK
RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP
EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG
QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS
QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT
QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA
GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS
NSRVSEPHRS IFPEMHSDSA SKDVPGRILL DIDNDTESTA L
